IF2_NOCSJ
ID IF2_NOCSJ Reviewed; 938 AA.
AC A1SLK7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Noca_3190;
OS Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC Nocardioides.
OX NCBI_TaxID=196162;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; CP000509; ABL82692.1; -; Genomic_DNA.
DR RefSeq; WP_011756626.1; NC_008699.1.
DR AlphaFoldDB; A1SLK7; -.
DR SMR; A1SLK7; -.
DR STRING; 196162.Noca_3190; -.
DR PRIDE; A1SLK7; -.
DR EnsemblBacteria; ABL82692; ABL82692; Noca_3190.
DR KEGG; nca:Noca_3190; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_4_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000640; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..938
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008290"
FT DOMAIN 431..603
FT /note="tr-type G"
FT REGION 55..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..447
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 465..469
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 490..493
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 544..547
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 580..582
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 116..140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 440..447
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 490..494
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 544..547
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 938 AA; 98291 MW; 7BBD39D7B5DF10A8 CRC64;
MAKTRVHELA KEFGVESKFV LEKFKEMGEF VKSASSTVEL PAEMRFRKEY GEKLKAEASA
APAAPAEKPA AKKAPAKKAA ATAEPEALAA EPAAEPAAAE APAAAEAEAP AAKAAAPKPG
PKPAPVAEQP APPAEPEAPE APEAPAASAA PAAPKAPAPR PVGRPGAPRP GNNPFASSQG
MGRRPAPGAP AAPGAGDNRP PRPPAAREGG VPGRPGMPRP NPAMMPKSPS AFGAGPGGRG
PARPGAPGRG GAPGRGGAPG RGGVGTGAPG RGGAPGGGFG PSGGGRPGGG RPGQRGQTQG
AFGRPGGPSR RGRKSKRARR QEFEAMEAPT IGGIRVRKGN GETVRLPRGA SLTDFAERIN
VEPAQLVQML FSLGEMVTAT ESVNDETLEL LGEELNYVVE VVSPEDEDRE LLESFDIEFA
DDEDDEGHFE ARPPVVTVMG HVDHGKTKLL DALRHANVAS GEAGGITQHI GAYQVHTDVD
GEDRKITFID TPGHEAFTAM RARGSQSSDI AVLVVAADDG VMPQTVEALN HAKAAGVPIV
VAVNKIDKPE ADPTKVRGQL TEYGLVPEEY GGDTMFVDVS AKSELNLDKL LEAVVLTADA
SLDLRANPNR DAQGLVIEAH LDRGRGPVAT ILVQRGTLHV GDSIVAGPAH GRVRAMLDEY
GNELTEATPS RPAMVLGLST VPGAGQNFIV VEDDRMARQI AEKREARERA AMQAKRRVRR
TLEDFMASME KGESQELNLI LKGDVSGSVE ALEDALAKID VGDDVSLRVI DRGVGAITET
NVDLAAASDA IIIGFNVRPQ GKATELADRE GVEIRYYTVI YQAIEEIEAA LKGMLKPEFE
ESTLGQAEIR AIFRSSKVGN IAGCMVISGV IRRNAKVRVI RDGAVVADNL DLASLKREKD
DASEVREGFE CGLVLRNFQD IKEGDIVEAF EMREIPRA
